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Polysaccharide Lyase Family 32

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Substrate specificities

The PL32 family was created following the functional characterization of the ORF “HMPREF1071_02769” from Bacteroides salyersiae CL02T12C01 (EIY62149.1), which showed endo-mannuronan lyase activity (EC 4.2.2.3) [1]. Shortly afterwards, the sequence was reclassified as PL_nc on the basis of structural modelling revealing that the catalytic domain was restricted to the N-terminal domain (PL_nc) [2]. The small number of sequences and the proximity to the PL14 and PL36 families do not allow the creation of a new PL family.


References

  1. Helbert W, Poulet L, Drouillard S, Mathieu S, Loiodice M, Couturier M, Lombard V, Terrapon N, Turchetto J, Vincentelli R, and Henrissat B. (2019). Discovery of novel carbohydrate-active enzymes through the rational exploration of the protein sequences space. Proc Natl Acad Sci U S A. 2019;116(13):6063-6068. DOI:10.1073/pnas.1815791116 | PubMed ID:30850540 [Helbert2019]
  2. Drula E, Garron ML, Dogan S, Lombard V, Henrissat B, and Terrapon N. (2022). The carbohydrate-active enzyme database: functions and literature. Nucleic Acids Res. 2022;50(D1):D571-D577. DOI:10.1093/nar/gkab1045 | PubMed ID:34850161 [Drula2022]

All Medline abstracts: PubMed